(data stored in SCRATCH zone)

SWISSPROT: Q13S05_PARXL

ID   Q13S05_PARXL            Unreviewed;      1146 AA.
AC   Q13S05;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
DE            Short=GMPMT {ECO:0000256|HAMAP-Rule:MF_02124};
DE            EC=2.4.99.16 {ECO:0000256|HAMAP-Rule:MF_02124};
DE   AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
GN   Name=glgE {ECO:0000256|HAMAP-Rule:MF_02124};
GN   ORFNames=Bxe_B2861 {ECO:0000313|EMBL:ABE33134.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33134.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33134.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33134.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P)
CC       as the sugar donor to elongate linear or branched alpha-(1->4)-
CC       glucans. Is involved in a branched alpha-glucan biosynthetic
CC       pathway from trehalose, together with TreS, Mak and GlgB.
CC       {ECO:0000256|HAMAP-Rule:MF_02124}.
CC   -!- CATALYTIC ACTIVITY: Alpha-maltose 1-phosphate + ((1->4)-alpha-D-
CC       glucosyl)(n) = phosphate + ((1->4)-alpha-D-glucosyl)(n+2).
CC       {ECO:0000256|HAMAP-Rule:MF_02124}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02124}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02124}.
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DR   EMBL; CP000271; ABE33134.1; -; Genomic_DNA.
DR   RefSeq; WP_011490514.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S05; -.
DR   STRING; 266265.Bxe_B2861; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABE33134; ABE33134; Bxe_B2861.
DR   GeneID; 4006774; -.
DR   KEGG; bxb:DR64_5190; -.
DR   KEGG; bxe:Bxe_B2861; -.
DR   PATRIC; fig|266265.5.peg.4830; -.
DR   eggNOG; ENOG4105EP6; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000239230; -.
DR   KO; K16147; -.
DR   OMA; QDIVNPD; -.
DR   OrthoDB; POG091H0A4R; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.60.40.10; -; 1.
DR   HAMAP; MF_02124; GlgE; 1.
DR   InterPro; IPR026585; GlgE.
DR   InterPro; IPR021828; GlgE_dom_N/S.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10357:SF191; PTHR10357:SF191; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF11896; DUF3416; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q13S05.
DR   SWISS-2DPAGE; Q13S05.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02124};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02124}.
FT   DOMAIN      666   1011       Aamy. {ECO:0000259|SMART:SM00642}.
FT   REGION      986    987       Maltose 1-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02124}.
FT   ACT_SITE    846    846       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_02124}.
FT   ACT_SITE    875    875       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02124}.
FT   BINDING     714    714       Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02124}.
FT   BINDING     774    774       Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02124}.
FT   BINDING     809    809       Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02124}.
FT   BINDING     847    847       Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02124}.
FT   SITE        933    933       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_02124}.
SQ   SEQUENCE   1146 AA;  126939 MW;  64C40AD3BE7999FE CRC64;
     MESPNGYAPR IYFFHSLLVG PLDAWPAQFA HAAGLGFDHA LIGSLFEPGQ AGHGQVVGNH
     ARLHPVFEAQ QPATEAIRTL ANAAAQNGLT LLADLVIDRM AADGALYAEH ADWFHPFESE
     EARLDPRHVH REDNVAYANF NDPGSSAALA GWWTQQLLTL ADAGVGGFRF DSPHRVPGAV
     WRQLRDAVRA KHPEVRFLAA TPGLAREDLR GLEGAGFDSV FSSVRWWDFR SSWMVEEHAA
     LARIGAPIAF PEAPYGTRLA AELSDAHDAA IVERAYRRAL FASVAIGTGW MMPMGFEYGI
     TEPMSQTRGD ASQFALAAQA KQFDLSERIT HVNQVVRNTK TLHANGELRP LSGPGAPAAI
     LLRADQPDLR DAREAVLIAI NPELGAPLRV DPARFLAGVP GNFTRFVPLD APANASPATL
     TPFTLAPGAV RLLRAVAEKP IRLAPPIDKA NSKRSGRKTV LEAINAPRVA IESVTPSVDN
     GRFAAKRTVG EHAEITAAIF AEGHDKIAAA VIWRAADETA WHEVPMTPAE PAGLDIWKAR
     IPLERLGRHE FTVIAWRDDF ASLVEHIQKK LKAGQTVELE LDEAAHLFAL VLAEVETSEG
     AVTAPLEHIV KEFTKADAET KLALLLAPTT ARAMTAARHR PFLSRDPVIY KIDADRTAAR
     FASWYEIFPR SMSDDESRHG TFADVTKKLP RIRDMGFDVL YFPPIHPIGV ANRKGRNNTL
     NAQPGDVGSP YAIGGVEGGH TAVHPQLGTL DDFKAMLAAA HEHGLEIALD FAVQCSPDHP
     WLKEHPTWFA WRPDGTLRYA ENPPKKYQDI VNPDFYAHDA KPDLWLALRD VFLFWIEAGV
     HIFRIDNPHT KPLPFWEWVI GDIRARYPDT IFLAEAFTRP RMMNRLGKIG FSQSYTYFTW
     RESKRDFIEY MTELTQTGAR DSYRPNFFVN TPDINPRHLQ SQGRTGFLIR AALASTLAGL
     WGVYSGFELC EAAALPNSEE YLDSEKYQLR AWDWNRPGNI VGEISALNRI RRANPALQTH
     LGLTFLPAHN DNVLFFEKAT ESRDNVIVVA INLDPFNEQG ADIELSWETF QKWNLPDHGP
     LEVTDQMTGA RFEWHGRWQH VQLGSGQPFS IWRIAPLGGL PAERPDEADS DYHADAGNPT
     PTEGAT
//

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